Structural and functional consequences of removing the N-terminal domain from the magnesium chelatase ChlH subunit of Thermosynechococcus elongatus.
about
Crystal structure of the catalytic subunit of magnesium chelatasePorphyrin Binding to Gun4 Protein, Facilitated by a Flexible Loop, Controls Metabolite Flow through the Chlorophyll Biosynthetic Pathway.Nanomechanical and Thermophoretic Analyses of the Nucleotide-Dependent Interactions between the AAA(+) Subunits of Magnesium Chelatase.Organization of chlorophyll biosynthesis and insertion of chlorophyll into the chlorophyll-binding proteins in chloroplasts.CHLH/GUN5 Function in Tetrapyrrole Metabolism Is Correlated with Plastid Signaling but not ABA Responses in Guard Cells.
P2860
Structural and functional consequences of removing the N-terminal domain from the magnesium chelatase ChlH subunit of Thermosynechococcus elongatus.
description
2014 nî lūn-bûn
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年论文
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2014年论文
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2014年论文
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name
Structural and functional cons ...... Thermosynechococcus elongatus.
@en
type
label
Structural and functional cons ...... Thermosynechococcus elongatus.
@en
prefLabel
Structural and functional cons ...... Thermosynechococcus elongatus.
@en
P2093
P2860
P356
P1433
P1476
Structural and functional cons ...... Thermosynechococcus elongatus
@en
P2093
Amanda A Brindley
C Neil Hunter
Christopher J Marklew
Paul A Davison
Per A Bullough
P2860
P304
P356
10.1042/BJ20140463
P407
P577
2014-12-01T00:00:00Z